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Information on EC 5.4.2.12 - phosphoglycerate mutase (2,3-diphosphoglycerate-independent) and Organism(s) Geobacillus stearothermophilus and UniProt Accession Q9X519

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EC Tree
IUBMB Comments
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
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Geobacillus stearothermophilus
UNIPROT: Q9X519
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Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ipgam, cofactor-independent phosphoglycerate mutase, 3-phosphoglycerate mutase, independent pgm, independent pgam, sso0417, 2,3-biphosphoglycerate-independent phosphoglycerate mutase, co-factor-independent phosphoglycerate mutase, cofactor independent phosphoglycerate mutase, ph0037, more
SYSTEMATIC NAME
IUBMB Comments
D-phosphoglycerate 2,3-phosphomutase (2,3-diphosphoglycerate-independent)
The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. cf. EC 5.4.2.11 phosphoglycerate mutase (2,3-diphosphoglycerate-dependent). The enzyme contains two Mn2+ (or in some species two Co2+ ions). The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. Both metal ions are involved in the reaction.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
?
show the reaction diagram
-
-
-
?
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
2-phospho-D-glycerate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.4
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
pH 7.4, 1 mM Mn2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1500
methionyl-phosphoglycerate mutase
500
selenomethionyl-phosphoglycerate mutase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
2% and 22% of maximal activity at pH 6.0 and pH 7.0, respectively, at 1 mM Mn2+
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GPMI_GEOSE
511
0
57003
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of iPGM complexed with 3-phosphoglycerate and Mn2+ at 1.9 A resolution
methionyl and selenomethionyl phosphoglycerate mutase, vapor drop hanging diffusion, mixing equal volumes of protein solution, i.e. 50 mg/ml protein in 150 mM 3-phosphoglycerate, pH 7.4 and reservoir solution containing 2 M ammonium sulfate, 25 mM zinc acetate, 20 mM cesium chloride, 15 mM 2-mercaptoethanol, 3% polyethylene glycol 200 and 50 mM Tris-HCl, pH 7.4, crystals diffract to 2.5 A resolution
crystals of wild-type and S62A mutant at 1.4 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H123N
3% of wild-type activity
H125N
67% of wild-type activity
H128N
20% of wild-type activity
H42N
91% of wild-type activity
H42N/H128N
8% of wild-type activity
H445N
18% of wild-type activity
H462N
0.3% of wild-type activity
H66N
2% of wild-type activity
S62A
-
no phosphoglycerate mutase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant phosphoglycerate mutase
recombinant phosphoglycerate mutase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of native and selenomethionyl phosphoglycerate mutase in Escherichia coli
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jedrzejas, M.J.; Chander, M.; Setlow, P.; Krishnasamy, G.
Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus
EMBO J.
19
1419-1431
2000
Geobacillus stearothermophilus (Q9X519)
Manually annotated by BRENDA team
Rigden, D.J.; Lamani, E.; Mello, L.V.; Littlejohn, J.E.; Jedrzejas, M.J.
Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling
J. Mol. Biol.
328
909-920
2003
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Chander, M.; Setlow, P.; Lamani, E.; Jedrzejas, M.J.
Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus
J. Struct. Biol.
126
156-165
1999
Geobacillus stearothermophilus (Q9X519)
Manually annotated by BRENDA team